Abstract:
:A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bennett EP,Hassan H,Hollingsworth MA,Clausen Hdoi
10.1016/s0014-5793(99)01268-5keywords:
subject
Has Abstractpub_date
1999-10-29 00:00:00pages
226-30issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01268-5journal_volume
460pub_type
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